Affinity chromatography will be our principal technique for the purification of human interferon. We will use two systems of affinity chromatography based on hydrophobic interaction and carbohydrate recognition by concanavalin A. Hydrophobic chromatography will be done on serum albumin immobilized directly to an agarose matrix or through molecular arms. In addition, hydrophobic chromatography will be done on hydrocarbon arms (of varied chain length) attached to agarose. Chromatography on conavalin A-agarose will be further developed by immobolization of the lectin in its dimeric and tetrameric forms through a molecular arm. We will also include isoelectrofocusing in our purification scheme, as an additional technique of high resolution potential. This novel purification scheme should allow us to develop human interferon of sufficient purity that structure-function studies and clinical investigations, of a quality never-before-entertained, can be accomplished.